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  • Title: Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm.
    Author: Nakamoto H, Bardwell JC.
    Journal: Biochim Biophys Acta; 2004 Nov 11; 1694(1-3):111-9. PubMed ID: 15546661.
    Abstract:
    Disulfide bond formation is a catalyzed process in vivo. In prokaryotes, the oxidation of cysteine pairs is achieved by the transfer of disulfides from the highly oxidizing DsbA/DsbB catalytic machinery to substrate proteins. The oxidizing power utilized by this system comes from the membrane-embedded electron transport system, which utilizes molecular oxygen as a final oxidant. Proofreading of disulfide bond formation is performed by the DsbC/DsbD system, which has the ability to rearrange non-native disulfides to their native configuration. These disulfide isomerization reactions are sustained by a constant supply of reducing power provided by the cytoplasmic thioredoxin system, utilizing NADPH as the ultimate electron source.
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